Primary structure and kinetic interaction with glycoproteins of the lectin from seeds of Cratylia floribunda

被引：0

作者：

Cavada, BS

Nogueira, NAP

Farias, CMSA

Grangeiro, TB

Ramos, MV

Thole, HH

Raida, M

Rougé, P

Calvete, JJ

机构：

[1] Univ Fed Ceara, Dept Biol, BR-451970 Fortaleza Ceara, Brazil

[2] Univ Fed Ceara, Dept Biochem & Mol Biol, BR-451970 Fortaleza Ceara, Brazil

[3] Kinderklin Medizin Hsch, D-30623 Hannover, Germany

[4] Niedersachs Inst Pedtidforschung GmbH, D-30635 Hannover, Germany

[5] CSIC, Inst Biomed Valencia, Valencia 46010, Spain

[6] Inst Pharmacol & Biol Structurale, CNRS, UPR 9062, F-31077 Toulouse, France

来源：

PROTEIN AND PEPTIDE LETTERS | 1999年 / 6卷 / 01期

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The complete 236-amino-acid sequence of the glucose/mannose specific lectin from seeds of Cratylia floribunda (CFL) was determined by automated Edman sequencing of overlapping proteolytic peptides purified by HPLC after digestion of the lectin with endoproteinases Lys-C, Asp-N, trypsin and chymotrypsin. Mass spectrometry confirmed the sequence analysis and showed that CFL consists of a mixture of full length, single-chain polypeptide (alpha-chain. 25397 +/- 3 Da) and its' noncovalently associated beta (residues 1-118, 12847 +/- 2 Da) and gamma (residues 119-236, 12568 +/- 1 Da) fragments. The primary structure of Cratylia floribunda lectin has extensive amino acid sequence homology with those of lectins from species of the taxonomically related genera Canavalia and Dioclea. However, using surface plasmon resonance, CFL and ConA, the seed lectin from Canavalia ensiformis, displayed distinct kinetic interactions with glycoproteins, indicating structural differences in their extended glycan binding-sites.

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页码：27 / 34

页数：8

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